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Database: UniProt
Entry: A0A3N5AYJ2_9BACI
LinkDB: A0A3N5AYJ2_9BACI
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ID   A0A3N5AYJ2_9BACI        Unreviewed;       758 AA.
AC   A0A3N5AYJ2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE            EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN   ORFNames=EDC24_2864 {ECO:0000313|EMBL:RPF50049.1};
OS   Aquisalibacillus elongatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aquisalibacillus.
OX   NCBI_TaxID=485577 {ECO:0000313|EMBL:RPF50049.1, ECO:0000313|Proteomes:UP000276443};
RN   [1] {ECO:0000313|EMBL:RPF50049.1, ECO:0000313|Proteomes:UP000276443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18090 {ECO:0000313|EMBL:RPF50049.1,
RC   ECO:0000313|Proteomes:UP000276443};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC       Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000206,
CC         ECO:0000256|RuleBase:RU003410};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, ECO:0000256|RuleBase:RU003410}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family. {ECO:0000256|ARBA:ARBA00010406,
CC       ECO:0000256|RuleBase:RU003410}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RPF50049.1}.
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DR   EMBL; RKRF01000014; RPF50049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N5AYJ2; -.
DR   OrthoDB; 9762933at2; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000276443; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   CDD; cd01679; RNR_I; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR013346; NrdE_NrdA_C.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   InterPro; IPR039718; Rrm1.
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR   PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR   PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 1.
DR   Pfam; PF00317; Ribonuc_red_lgN; 1.
DR   PRINTS; PR01183; RIBORDTASEM1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR   PROSITE; PS00089; RIBORED_LARGE; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW   ECO:0000256|RuleBase:RU003410};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003410};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276443}.
FT   DOMAIN          616..638
FT                   /note="Ribonucleotide reductase large subunit"
FT                   /evidence="ECO:0000259|PROSITE:PS00089"
SQ   SEQUENCE   758 AA;  87098 MW;  CB19A153BF87D52B CRC64;
     MTVKTEPIIV TEGGVYQERF DEQQLRDYLL GLLIDFEELD GATFTEKIIQ SVITKESITK
     EQITNEVLLR GLENISPEEP NWTYVCSRVY LDQLYKKASL NRGYSRMQKY GNLYELTRYL
     TKINIFSDQL LTYYDQNEFE ELASIIEPER DQLFTYIGIR TLADRYLAKD HEGRIYELPQ
     ERFLIIAMSL MIYEPKEKRL DLVKEAYWAM SNLYMTVATP TLSNAGKAHG QLSSCFIDTV
     DDSLQGIYDS NTDIANLSKN GGGIGVYLGK IRSHGSSIKG FKGISSGVMP WMKQLNNTAV
     SVDQLGQRQG AIAVYLDVWH KDIHKFLDAK LNNGDERQRT HDLFTGVTLP DLFMEKVEAR
     ENWYLFDPHE VREVMGYSLE DYYDEEDGKG SFREKYEECV NHQGLSKEEV PAIDLMKRIM
     ISQLETGTPF MFYRDEVNRK NPNRHKGMIY SSNLCTEITQ NQSPTTVEEQ FTEDGKIIVT
     KNPGDFVVCN LSSINLGKAV TSGVLERLIP IQVRMLDNVI DLNDIPVLQA QIANQKYRAV
     GLGTFGYHHL LALIGFRWES EEAVEFADHL YEQIAYLTIK ASNDLAKEKG AYPSFEGSDW
     SNGQYFEKRG YHSPEWNKLK EKVQKHGVRN GYLMAVAPNS STSLIAGSTA SIDPIFKKFY
     SEEKKDYKIP VTAPDLSPKT FWLYKSAYDI DHQWTIKQNE ARQKHIDQSI SFNFYVRNNI
     KAKELLDLHL SAWKSKFKTT YYTRSTSSEI EDCVSCES
//
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